Calnexin, an abundant ~90kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90 (1). It consists of a large 50kDa N-terminal calcium-binding luminal domain, a single transmembrane helix and a short acidic cytoplasmic tail (2, 3). Unlike its ER counterparts which have a KDEL sequence on their C-terminus to ensure ER retention (4), calnexin has positively charged cytosolic residues that do the same thing (3). Most ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into multi-subunit proteins. Calnexin together with calreticulin, plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their mono-glycosylated glycans (5, 6). Calnexin has also been shown to associate with the major histocompatibility complex class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin (7).

Calnexin, an abundant ~90kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90 (1). It consists of a large 50kDa N-terminal calcium-binding luminal domain, a single transmembrane helix and a short acidic cytoplasmic tail (2, 3). Unlike its ER counterparts which have a KDEL sequence on their C-terminus to ensure ER retention (4), calnexin has positively charged cytosolic residues that do the same thing (3). Most ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into multi-subunit proteins. Calnexin together with calreticulin, plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their mono-glycosylated glycans (5, 6). Calnexin has also been shown to associate with the major histocompatibility complex class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin (7).

Calnexin, an abundant ~90kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90 (1). It consists of a large 50kDa N-terminal calcium-binding luminal domain, a single transmembrane helix and a short acidic cytoplasmic tail (2, 3). Unlike its ER counterparts which have a KDEL sequence on their C-terminus to ensure ER retention (4), calnexin has positively charged cytosolic residues that do the same thing (3). Most ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into mulit-subunit proteins. Calnexin together with calreticulin, plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their mono-glycosylated glycans (5, 6). Calnexin has also been shown to associate with the major histocompatibility complex class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin (7).

Product Type:

Antibodies

Format:

Rabbit Antiserum

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu | Ms | Rt | Bv | Ck | Dg | GP | Hm | Pg | Mk | Rb | Sh | Xe

Immunogen:

A 19 residue synthetic peptide based on dog calnexin and the peptide coupled to KLH

Calnexin, an abundant ~90kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90 (1). It consists of a large 50kDa N-terminal calcium-binding luminal domain, a single transmembrane helix and a short acidic cytoplasmic tail (2, 3). Unlike its ER counterparts which have a KDEL sequence on their C-terminus to ensure ER retention (4), calnexin has positively charged cytosolic residues that do the same thing (3). Most ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into mulit-subunit proteins. Calnexin together with calreticulin, plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their mono-glycosylated glycans (5, 6). Calnexin has also been shown to associate with the major histocompatibility complex class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin (7).

Product Type:

Antibodies

Format:

Rabbit Antiserum

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu | Ms | Rt | Bv | Ck | Dg | GP | Hm | Pg | Mk | Rb | Sh | Xe

Immunogen:

A 19 residue synthetic peptide based on dog calnexin and the peptide coupled to KLH

Calnexin, an abundant ~90kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90 (1). It consists of a large 50kDa N-terminal calcium-binding luminal domain, a single transmembrane helix and a short acidic cytoplasmic tail (2, 3). Unlike its ER counterparts which have a KDEL sequence on their C-terminus to ensure ER retention (4), calnexin has positively charged cytosolic residues that do the same thing (3). Most ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into multi-subunit proteins. Calnexin together with calreticulin, plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their mono-glycosylated glycans (5, 6). Calnexin has also been shown to associate with the major histocompatibility complex class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin (7).

Calnexin, an abundant ~90kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90 (1). It consists of a large 50kDa N-terminal calcium-binding luminal domain, a single transmembrane helix and a short acidic cytoplasmic tail (2, 3). Unlike its ER counterparts which have a KDEL sequence on their C-terminus to ensure ER retention (4), calnexin has positively charged cytosolic residues that do the same thing (3). Most ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into multi-subunit proteins. Calnexin together with calreticulin, plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their mono-glycosylated glycans (5, 6). Calnexin has also been shown to associate with the major histocompatibility complex class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin (7).

ERK1 or MAPK3 is ubiquitously expressed protein serine/threonine kinase involved in regulating cellular differentiation and proliferation in response to extracellular mitogens or growth factors. MAPK3 is activated by upstream signalling by monomeric G-proteins. MAPK3 activation leads to its translocation from the cytosol to the nucleus where it can target substrate proteins involved in cell cycle regulation; Cyclin D1, suppression of apoptosis; BCL2 and BAD, tumour supression; p53, cell migration; PAI-1, and MHCII mediated immune response; PPARg1. Dysfunction of MAPK3 expression and activity has been observed in a variety of cancers. Predominantly overexpression of MAPK3 or constitutive activation has been observed in cancer cell lines. Activation of MAPK3 does not appear to be due to mutations in the protein itself but rather aberrant signalling in upstream factors including Raf, Ras and epidermal growth factor receptor. MAPK3 may also have a role in promoting metastasis in invasive tumours.

DUSP3 is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli.

Product Type:

Antibodies

Format:

PBS pH7.4, 50% glycerol, 0.025% Thimerosal

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu | Ms

Immunogen:

A synthetic peptide corresponding to the N-terminal of human DUSP3 (AA 6-19)

Applications:

WB | AM

Application Details:

WB (1:250); optimal dilutions for assays should be determined by the user.

DUSP3 is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli.

Product Type:

Antibodies

Format:

PBS pH7.4, 50% glycerol, 0.025% Thimerosal

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu | Ms

Immunogen:

A synthetic peptide of human DUSP3 (AA 144-158)

Applications:

WB | AM

Application Details:

WB (1:250); optimal dilutions for assays should be determined by the user.

DUSP3 is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli.

Product Type:

Antibodies

Format:

PBS pH7.4, 50% glycerol, 0.025% Thimerosal

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu | Ms

Immunogen:

A synthetic peptide corresponding to the C-terminal of human DUSP3 (AA 171-185)

Applications:

WB | AM

Application Details:

WB (1:250); optimal dilutions for assays should be determined by the user.

The Glutathione S-Transferase (GST) family of isozymes function to detoxify and neutralize a wide variety of electrophilic molecules by mediating their conjugation with reduced glutathione (1). Human GSTs are encoded by 5 gene families, expressing in almost all tissues as four cytosolic and one microsomal forms. Dividing the family by isoelectric points, the basic alpha (pI 811), the neutral mu (pI 57) and acidic pi (pH<5) classes are populated by additional subclasses, each isozyme displaying differential specificity for given electrophilic molecules (2). Given its pivotal role in ameliorating oxidative stress/damage, GST activity has been repeatedly investigated as a biomarker for arthritis, asthma, COPD, and multiple forms of cancer, as well as an environmental marker (3-7). Examination of GST isoforms and activity in human cancers, tumors and tumor cell lines has revealed the predominance of the acidic pi class. Furthermore, this activity is thought to substantially contribute to the innate or acquired resistance of specific neoplasms to anticancer therapy (8,9).

Product Type:

Assay Kits

Storage Temp:

4ºC

Species Reactivity:

Hu | Mlsk | Fs

Applications:

Fluorometric assay used to quantitatively measure the activity of glutathione S-transferase in samples.

The Glutathione S-Transferase Activity kit is designed to quantitatively measure the activity of GST present in a variety of samples. A GST standard is provided to generate a standard curve for the assay and all samples should be read off the standard curve. The kit utilizes a non-fluorescent molecule that is a substrate for the GST enzyme which covalently attaches to glutathione (GSH) to yield a highly fluorescent product. Mixing the sample or standard with the supplied Detection Reagent and GSH and incubating at room temperature for 30 minutes yields a fluorescent product which is read at 460 nm in a fluorescent plate reader with excitation at 390 nm. The activity of the GST in the sample is calculated, after making a suitable correction for any dilution of the sample, using software available with most fluorescence plate readers. We have provided a 96 well plate for measurement but this assay is adaptable for higher density plate formats. The end user should ensure that their HTS black plate is suitable for use with these reagents prior to running samples.

Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

No confirmed exceptions from predicted reactivity are currently known.

Special application note:

Name of this antibody has been changed from L-30 | 50S ribosomal protein L30 to L7/L12 based on the following reference: Randolph-Anderson et al. (1989). Electrophoretic and immunological comparisons of chloroplast and prokaryotic ribosomal proteins reveal that certain families of large subunit proteins are evolutionarily conserved. J Mol Evol. 1989 Jul;29(1):68-88.

Iron-hydrogenase HydA2 is catalyzing reversible oxidation of molecular hydrogen. In Chlamydomonas the protein is present in low levels of 1 µg/liter of culture.Synonyme: HYD1/1

Product Type:

Antibody

Antibody Type:

Polyclonal

Format:

Lyophilized

Storage Temp:

Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

HydA1 (497aa) has a calculated MW of 53.1 kDa, but this is including the signal peptide, which gets cleaved off. The protein without TP has a calculated MW of 47.5 kDa and runs according to its size at about 48 kDa.HydA2 (505aa) has a calculated MW of 53.7 kDa, but this is including the signal peptide, which gets cleaved off. The protein without TP can only be estimated, since the cleavage site is known only from in silico analysis. It has a calculated MW of 47.3 kDa and should run in the gel also according to its size.This antibody is binding recombinant HydA1/2 protein.

In Chlamydomonas HydA is present in low levels of 1 µg/liter of culture. Therefore, an induction of cells by anaerobic adaptation or sulfur depravation (10 x higher amount than with anaerobic adaptation) is necessary for successful detection using this antibody. Methods of HydA induction are described in Hemschemeier et al. 2009.To detect HydA1/A2 in Chlamydomonas extracts amount loaded per well corresponds to 2 µg of chlorophyll for sulfur deprived cells, where relatively much HydA1 is synthesized or corresponds to 2-4 µg of artificially anaerobic induced cultures, where the HydA1 protein level is lower. This antibody is recognizing 1 ng of recombinant HydA protein.

Tubulin alpha (TUA) together with beta tubulin is making up microtubules.

Product Type:

Antibody

Antibody Type:

Polyclonal

Format:

Lyophilized

Storage Temp:

Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

The clone MYG13 recognizes CD22 cell surface antigen, a 130-140kDa protein. The expression of CD22 is primarily restricted to the normal and neoplastic B cells but does not express on other hematopoietic cells. The initiation of expression of CD22 starts in the cytoplasm of pro-B and pre-B cells. Although CD22 is not expressed by plasma cells, it is abundantly expressed by the follicular mantle and marginal zone B-cells. Being a member of the immunoglobulin superfamily, CD22 serves as an adhesion receptor for sialic acid-bearing ligands expressed on erythrocytes and leukocytes. The role of CD22 in the activation of B-cells is primarily associated with tyrosine kinases mediated signal transduction pathways.

Western blot (WB) at a suggested dilution of 1:2,000 - 1:6,000. Immunohistochemistry (IHC) and Immunofluorescence (IF). Biosensis recommends optimal dilutions/concentrations should be determined by the end user.

Alternative Names:

ARMET, ARP

Accession Number:

P55145

Reconstitution:

Store antibody stock solution at +4°C upon receipt. DO NOT FREEZE. This product is an (NH4)2SO4 precipitate. To use, mix well by pipetting or vortexing gently prior use, then withdraw the desired amount of antibody stock solution and dilute into your antibody dilution buffer and use normally. Alternatively, material can be centrifuged at 10K x g for 5 minutes and the liquid sulfate solution carefully removed. Then precipitated antibody can be resuspended in 0.1M P, 250mM NaCL, pH 7.4 solution. The solution should then be divided into working aliquots and stored at -80C until used. Prevent multiple freeze thaw cycles of aliquots for best product life.

Shelf Life:

12 months after purchase

Specificity:

MANF (Mesencephalic astrocyte-derived neurotrophic factor). No cross-reactivity in MANF-knockout mouse. No cross-reactivity with CDNF in IHC, slightly cross-reacts with purified CDNF in WB. | No cross-reactivity with CDNF in IHC, slightly cross-reacts with purified CDNF in WB.

Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6.

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